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Myeloperoxidase binds to non-vital spermatozoa on phosphatidylserine epitopes

Myeloperoxidase binds to non-vital spermatozoa on phosphatidylserine epitopes
Myeloperoxidase binds to non-vital spermatozoa on phosphatidylserine epitopes
The heme protein myeloperoxidase is released from stimulated polymorphonuclear leukocytes, a cell species found in increasing amounts in the male and female genital tract of patients with genital tract inflammations. Myeloperoxidase binds only to a fraction of freshly prepared human spermatozoa. The number of spermatozoa able to bind myeloperoxidase raised considerably in samples containing pre-damaged cells or in acrosome-reacted samples. In addition, myeloperoxidase released from zymosan-stimulated polymorphonuclear leukocytes was also able to bind to pre-damaged spermatozoa. The ability of spermatozoa to bind myeloperoxidase coincided with the binding of annexin V to externalized phosphatidylserine epitopes indicating the loss of plasma membrane integrity and with the incorporation of ethidium homodimer I. Myeloperoxidase did not interact with intact spermatozoa. Annexin V and myeloperoxidase bind to the same binding sites as verified by double fluorescence techniques, flowcytometry analyses as well as competition experiments. We demonstrated also that myeloperoxidase is eluted together with pure phosphatidylserine liposomes or liposomes composed of phosphatidylserine and phosphatidylcholine in gel filtration, but not with pure phosphatidylcholine liposomes. In conclusion, myeloperoxidase interacts with apoptotic spermatozoa via binding to externalized phosphatidylserine indicating a yet unknown role of this protein in recognition and removal of apoptotic cells during inflammation
1360-8185
1803-1812
Leßig, Jacqueline
0e9efb68-ba32-41b3-8a3e-4bb9c1fcf5dd
Spalteholz, Holger
45d20d07-51a1-4bd0-b1a4-679e06252380
Reibetanz, Uta
ac641146-8f5b-46ae-8008-641b73fe72e6
Salavei, Pavel
0d1e5dcf-34c4-4c3c-88b3-f7c09415dd5e
Fischlechner, Martin
b3930129-0775-4c05-81c7-475934df97ee
Glander, Hans-Jürgen
ff4e46e9-20e2-4f46-a016-149e0fdf63a7
Arnhold, Jürgen
e50bcd9c-311a-4671-bd59-9b66b47a2a75
Leßig, Jacqueline
0e9efb68-ba32-41b3-8a3e-4bb9c1fcf5dd
Spalteholz, Holger
45d20d07-51a1-4bd0-b1a4-679e06252380
Reibetanz, Uta
ac641146-8f5b-46ae-8008-641b73fe72e6
Salavei, Pavel
0d1e5dcf-34c4-4c3c-88b3-f7c09415dd5e
Fischlechner, Martin
b3930129-0775-4c05-81c7-475934df97ee
Glander, Hans-Jürgen
ff4e46e9-20e2-4f46-a016-149e0fdf63a7
Arnhold, Jürgen
e50bcd9c-311a-4671-bd59-9b66b47a2a75

Leßig, Jacqueline, Spalteholz, Holger, Reibetanz, Uta, Salavei, Pavel, Fischlechner, Martin, Glander, Hans-Jürgen and Arnhold, Jürgen (2007) Myeloperoxidase binds to non-vital spermatozoa on phosphatidylserine epitopes. Apoptosis, 12 (10), 1803-1812. (doi:10.1007/s10495-007-0113-5).

Record type: Article

Abstract

The heme protein myeloperoxidase is released from stimulated polymorphonuclear leukocytes, a cell species found in increasing amounts in the male and female genital tract of patients with genital tract inflammations. Myeloperoxidase binds only to a fraction of freshly prepared human spermatozoa. The number of spermatozoa able to bind myeloperoxidase raised considerably in samples containing pre-damaged cells or in acrosome-reacted samples. In addition, myeloperoxidase released from zymosan-stimulated polymorphonuclear leukocytes was also able to bind to pre-damaged spermatozoa. The ability of spermatozoa to bind myeloperoxidase coincided with the binding of annexin V to externalized phosphatidylserine epitopes indicating the loss of plasma membrane integrity and with the incorporation of ethidium homodimer I. Myeloperoxidase did not interact with intact spermatozoa. Annexin V and myeloperoxidase bind to the same binding sites as verified by double fluorescence techniques, flowcytometry analyses as well as competition experiments. We demonstrated also that myeloperoxidase is eluted together with pure phosphatidylserine liposomes or liposomes composed of phosphatidylserine and phosphatidylcholine in gel filtration, but not with pure phosphatidylcholine liposomes. In conclusion, myeloperoxidase interacts with apoptotic spermatozoa via binding to externalized phosphatidylserine indicating a yet unknown role of this protein in recognition and removal of apoptotic cells during inflammation

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Published date: 2007
Organisations: Organic Chemistry: SCF

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Local EPrints ID: 342561
URI: http://eprints.soton.ac.uk/id/eprint/342561
ISSN: 1360-8185
PURE UUID: d0913571-fe10-4add-8f56-631abe98a867

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Date deposited: 19 Oct 2012 07:54
Last modified: 14 Mar 2024 11:52

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Contributors

Author: Jacqueline Leßig
Author: Holger Spalteholz
Author: Uta Reibetanz
Author: Pavel Salavei
Author: Martin Fischlechner
Author: Hans-Jürgen Glander
Author: Jürgen Arnhold

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